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  • Pilin glycosylation in Neisseria meningitidis occurs by a similar pathway to wzy-dependent O-antigen biosynthesis in Escherichia coli.

    Author(s)
    Power, Peter M
    Seib, Kate L
    Jennings, Michael P
    Griffith University Author(s)
    Seib, Kate
    Jennings, Michael P.
    Year published
    2006
    Metadata
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    Abstract
    Pili (type IV fimbriae) of Neisseria meningitidis are glycosylated by the addition of O-linked sugars. Recent work has shown that PglF, a protein with homology to O-antigen 'flippases', is required for the biosynthesis of the pilin-linked glycan and suggests pilin glycosylation occurs in a manner analogous to the wzy-dependent addition of O-antigen to the core-LPS. O-Antigen ligases are crucial in this pathway for the transfer of undecraprenol-linked sugars to the LPS-core in Gram-negative bacteria. An O-antigen ligase homologue, pglL, was identified in N. meningitidis. PglL mutants showed no change in LPS phenotypes but did ...
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    Pili (type IV fimbriae) of Neisseria meningitidis are glycosylated by the addition of O-linked sugars. Recent work has shown that PglF, a protein with homology to O-antigen 'flippases', is required for the biosynthesis of the pilin-linked glycan and suggests pilin glycosylation occurs in a manner analogous to the wzy-dependent addition of O-antigen to the core-LPS. O-Antigen ligases are crucial in this pathway for the transfer of undecraprenol-linked sugars to the LPS-core in Gram-negative bacteria. An O-antigen ligase homologue, pglL, was identified in N. meningitidis. PglL mutants showed no change in LPS phenotypes but did show loss of pilin glycosylation, confirming PglL is essential for pilin O-linked glycosylation in N. meningitidis.
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    Journal Title
    Biochemical and Biophysical Research Communications
    Volume
    347
    Issue
    4
    DOI
    https://doi.org/10.1016/j.bbrc.2006.06.182
    Subject
    Medicinal and biomolecular chemistry
    Biochemistry and cell biology
    Bacteriology
    Medical biochemistry and metabolomics
    Publication URI
    http://hdl.handle.net/10072/62261
    Collection
    • Journal articles

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